CAZyme Information: MGYG000001354_00940

Basic Information

• Species: Bifidobacterium dentium
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium dentium
• CAZyme ID: MGYG000001354_00940
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
617	MGYG000001354_1|CGC25	68016.84	4.6271

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001354	2642081	Isolate	not provided	not provided

• Gene Location: Start: 1147156; End: 1149009 Strand: +

Full Sequence      

MWREDLPVNSLKKAFSMVAAAFAAVALMLMGAVPASALMDHSVDAVAGNDANADVVQADQ
DESSQTVMPDNPQAQLPDSVSESIPDSATVVSENLAVTAEGDVKDVETGETVTDPELVGT
EEQAPDPLAKTDGETFIPVAAADVKEAVDEADASAEQSQEQSSTDTDGKVTPAQFTSNEY
GAYWGSYNNTKAFFESGGNLFVQQAKGVIDVSQWQGNIDWAKAKADGVEGAIIRISYGWD
NGFDKTALRNISECKRLGIPFGIYTYSYSYDAATATAEGNDLVGLLKKAGVSPNDLSFPV
YYDLEQWTWTGHQVPTDPNVYNGIVNAWWGRLQAAGYNNLGVYSYMSYLNGPLNHGNIRS
KAKWVASYGPRTNFSYSANNRGWQYTSVGHVNGISGNVDMNAFGNREYVNPAAHWVTRNG
QKYWQDADGTYARGKEIFDPDSNAWYWIDSNGVMACNKDVYLRSNGGKWVRYDSNGHMVK
GEDYRYGGWYYFDTTTGAMAKGVKYISSNGGKKVYYDVITGKMAHGEVYLNYDKTHTGWY
LFDKTTGAMVYGDVYLRSNGGKWVRYDRSTGKMVKGLHKQNGAWYYFDETTGAMAHGRTW
VPEWEEWHTFDTITGRG

Enzyme Prediction     

No EC number prediction in MGYG000001354_00940.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	209	394	8.6e-36	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.04e-63	206	403	1	190	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599	GH25_muramidase	1.15e-27	208	403	2	186	Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
cd06523	GH25_PlyB-like	6.43e-25	208	402	2	176	PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd06522	GH25_AtlA-like	1.73e-24	208	401	3	189	AtlA is an autolysin found in Gram-positive lactic acid bacteria that degrades bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family includes the AtlA and Aml autolysins from Streptococcus mutans which have a C-terminal glycosyl hydrolase family 25 (GH25) catalytic domain as well as six tandem N-terminal repeats of the GBS (group B Streptococcus) Bsp-like peptidoglycan-binding domain. Other members of this family have one or more C-terminal peptidoglycan-binding domain(s) (SH3 or LysM) in addition to the GH25 domain.
cd06525	GH25_Lyc-like	4.54e-19	206	403	1	184	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADB10631.1	0.0	1	617	1	617
BAQ27936.1	0.0	1	617	1	617
VEG24607.1	0.0	1	617	1	617
QTL77697.1	0.0	1	617	1	617
QTL79551.1	0.0	1	617	1	617

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2WW5_A	1.20e-30	203	403	266	467	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A	2.95e-30	203	403	266	467	3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRT_A	1.27e-10	209	455	23	276	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRU_A	1.32e-09	209	403	23	207	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
3HMC_A	3.82e-08	208	419	7	191	Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	1.14e-08	209	403	12	196	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P25310	6.35e-07	209	403	85	279	Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000429	0.998785	0.000210	0.000194	0.000167	0.000151

TMHMM  Annotations     

start	end
13	35